Papio_anubisFamily: KH_1 Number of Genes: 40
Ensembl IDSymbolEntrez IDRBD RBPome PRIExpresion PathwayPhenotype ParalogOrthologGO
KHSRP
ANKHD1-EIF4EBP3
TDRKH
-
NOVA1
DDX43
KHDRBS3
MEX3C
-
IGF2BP2
PCBP1
HDLBP
FXR1
-
-
-
MEX3B
FMR1
ANKRD17
MEX3A
-
-
-
IGF2BP3
SF1
KHDRBS2
BICC1
-
ASCC1
AKAP1
-
-
IGF2BP1
PNPT1
KHDRBS1
PCBP3
NOVA2
-
FXR2
HNRNPK
MEX3D
-
FUBP3
PCBP4
PCBP2
-
-
-
-
-
-

Introduction

Pfam

KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.

InterPro

The K homology (KH) domain was first identified in the human heterogeneous nuclear ribonucleoprotein (hnRNP) K. It is a domain of around 70 amino acids that is present in a wide variety of quite diverse nucleic acid-binding proteins [PUBMED:8036511]. It has been shown to bind RNA [PUBMED:9302998, PUBMED:10369774]. Like many other RNA-binding motifs, KH motifs are found in one or multiple copies (14 copies in chicken vigilin) and, at least for hnRNP K (three copies) and FMR-1 (two copies), each motif is necessary for in vitro RNA binding activity, suggesting that they may function cooperatively or, in the case of single KH motif proteins (for example, Mer1p), independently [PUBMED:8036511].

Reference

  1. Burd CG, Dreyfuss G; , Science 1994;265:615-621.: Conserved structures and diversity of functions of RNA-binding proteins. PUBMED:8036511 EPMC:8036511 .

  2. Musco G, Stier G, Joseph C, Castiglione Morelli MA, Nilges M, Gibson TJ, Pastore A; , Cell 1996;85:237-245.: Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome. PUBMED:8612276 EPMC:8612276.